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Cited by 102Cholesterol and Lipid MetabolismReceptor Mechanisms and SignalingProtease and Inhibitor Mechanisms

Evidence for a second alpha 2-macroglobulin receptor.

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Misra, U.K., Chu, C.T., Gawdi, G., Pizzo, S.V.·1994·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)99909-6
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Abstract

alpha 2-Macroglobulin (alpha 2M)-methylamine binds to purified low density lipoprotein receptor-related protein (LRP), and it is assumed that LRP functions as the alpha 2M receptor in vivo. Binding of alpha 2M-methylamine to macrophage receptors elevates intracellular calcium ([Ca2+]i), inositol phosphates, and cyclic AMP. We have employed human alpha 2M-methylamine and recombinant receptor binding fragment (RBF) to study transduction mechanisms. Macrophages exposed to either ligand demonstrated a rapid rise in [Ca2+]i. Since the 39-kDa LRP/alpha 2M receptor-associated protein (RAP) blocks alpha 2M binding to LRP, we explored the effects of RAP upon signaling. Pretreatment of macrophages with RAP did not block the increase in [Ca2+]i elicited by alpha 2M-methylamine or RBF, suggesting a distinct binding site. RBF also elicited a transient 1.5-2.0-fold increase in inositol 1,4,5-triphosphate. In permeabilized macrophages, GTP gamma S and Gp-p(NH)p potentiated and sustained this inositol 1,4,5-triphosphate increase. Preincubation of permeabilized macrophages with GDP beta S abrogated the effects of GTP gamma S. Our results suggest that the signaling alpha 2M receptor is coupled to a pertussis toxin-insensitive G protein and possibly to a cholera toxin-sensitive G protein. We conclude that macrophages contain a second alpha 2M receptor that is G protein-coupled.

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  • Several ligands that interact with LRP are thought to initiate signaling events.

    “Interestingly, several ligands that are capable of interacting with LRP are also thought to initiate signaling events. These ligands include activated α2M (Misra et al., 1994), urokinase-type plasminogen activator (Nguyen et al., 1998), apolipoprotein E (Riddell et al., 1997) and tissue-type plasminogen activator (Hu et al., 2006).”

    From LRAD3, A Novel Low-Density Lipoprotein Receptor Family Member That Modulates Amyloid Precursor Protein Trafficking (2011) · cites this paper as Misra et al., 1994

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Authors
Misra, U. K., Chu, C. T., Gawdi, G., & Pizzo, S. V.
Affiliations
Duke Medical Center (US)
ORCID
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1994-04
Volume
269
Issue
17
Pages
12541-12547
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(18)99909-6
OpenAlex
W1482079857
Cited by
102
References
53
Citations by year
2021: 1 · 2019: 1 · 2018: 1 · 2015: 1 · 2014: 2 · 2013: 2 · 2012: 1
FWCI
9.71
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5p01ca029589-13)
  • National Heart, Lung, and Blood Institute (HL24066)
  • National Cancer Institute (CA29589)
Topics
  • Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
Keywords
alpha2-macroglobulin, alpha2-macroglobulin receptor, low density lipoprotein receptor-related protein, receptor-associated protein, macrophages, G protein-coupled receptor signaling, intracellular calcium, inositol 1,4,5-trisphosphate, pertussis toxin-insensitive G protein, signal transduction
MeSH terms
Cyclic AMP, Adenosine Diphosphate Ribose, alpha-Macroglobulins, Animals, Cholera Toxin, Humans, Inositol Phosphates, Methylamines, Mice, Inbred C57BL, Peptide Fragments, Virulence Factors, Bordetella, Proteins, Receptors, Immunologic, Signal Transduction, Macrophages, Peritoneal, GTP-Binding Proteins, Low Density Lipoprotein Receptor-Related Protein-1, Pertussis Toxin, Mice

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